High impact information on ARBP

• Furthermore, dimerization mutants show that, to bind ARBP efficiently, MAR sequences can act synergistically over large distances, apparently with the intervening DNA looping out [1].
• In mouse satellite DNA, use of several footprinting techniques characterized two high-affinity binding sites, whose sequences are related to the ARBP binding site consensus in the chicken lysozyme MAR (5'-GGTGT-3') [2].
• In band shift experiments, ARBP binds to two chicken repetitive sequences as well as to mouse satellite DNA with high affinity similar to that of its binding to chicken lysozyme MAR fragments [2].
• Band shift experiments indicated that methylation increased in vitro binding of ARBP to mouse satellite DNA two- to fivefold [2].
• However, a 452 bp subfragment (H1-HaeII), which still exhibits specific binding to nuclear matrices and contains two high-affinity binding sites for the abundant nuclear matrix protein ARBP, lost both of those abilities [3].

Biological context of ARBP

• High-affinity recognition of the identified DNA motif in MARs/SARs by ARBP is likely an important feature in the domain organization of chromatin [4].
• Nuclear matrix protein ARBP recognizes a novel DNA sequence motif with high affinity [4].
• Our results indicate that ARBP recognizes a novel DNA sequence motif containing the central sequence 5'-GGTGT-3' and flanking AT-rich sequences [4].
• A dimerized 177 bp sequence from fragment H1-HaeII, which also binds selectively to nuclear matrices and includes a duplicated ARBP binding site, was also unable to stimulate reporter gene expression [3].

Associations of ARBP with chemical compounds

• Here we characterize by DNase I footprinting, dimethyl sulfate protection, and mobility shift assays two binding sites for ARBP within a chicken lysozyme MAR fragment [4].

Analytical, diagnostic and therapeutic context of ARBP

• Here we show by gel filtration and gradient sedimentation that ARBP has an elongated shape [5].

References